Intracellular Camp(세포내 캠프)란 무엇입니까?
Intracellular Camp 세포내 캠프 - After the IM and dDAVP administrations, the rat kidneys were immunostained with AQP2 antibody, and intracellular cAMP was measured. [1] Our results indicate that activation SSTR2 by OCT can inhibit the activity of ASICs via an intracellular cAMP and PKA signaling pathway in rat DRG neurons. [2] More interestingly, we revealed that TRAF2 interacted with G protein-coupled receptor kinase (GRK2) in the cytoplasm of primary hFLS and helped to bring GRK2 to cell membrane in response of TNF-α stimulation, the complex of TRAF2 and GRK2 then separated on the membrane, and translocated GRK2 induced the desensitization and internalization of EP4, leading to reduced production of intracellular cAMP. [3] Recent reports indicate that intracellular cAMP-elevating compounds, including phosphodiesterases (PDE) inhibitors, may represent a promising class of anti-fibrotic agents. [4] Stimulation of intracellular cAMP with forskolin (FSK) and 3‐isobutyl‐1‐methylxanthine (IBMX) led to an increase in net oxalate secretion in the WT distal ileum and cecum and inhibition of sodium absorption in the cecum and distal colon. [5] PDE4 blocking can lead to increased levels of intracellular cAMP, which results in down-regulation of inflammatory responses by reducing the expression of tumor necrosis factor (TNF), interleukin (IL)-23, IL-17, interferon-γ, while increasing regulatory cytokines, such as IL-10. [6] PTS activity leads to reduced levels of intracellular cAMP, which in turn upregulate virulence genes. [7] Intracellular cAMP was studied in isolated islets using HTRF-based technology. [8] In the presence of both receptors, LPA2 and/or GPR55 activation facilitated co‐internalization, and activation of GPR55, uncoupled with Gαi, induced reduction of intracellular cAMP. [9] Upon sudden activation of β1-ARs in experiments, intracellular cAMP can transiently rise to a high concentration before converging to a steady state level. [10] Functionally, reduction of β3-AR lowered agonist-mediated increases in intracellular cAMP, lipolysis, and lipolysis-activated, uncoupling protein 1–mediated thermogenic capacity. [11] OT potentiated the KOR agonist-induced Gi/o protein-mediated decrease in intracellular cAMP, but did not affect the increase in KOR internalization caused by the KOR agonists dynorphin A and (-)-U-50488 hydrochloride (U50488). [12] After the IM and dDAVP administrations, the rat kidneys were immunostained with AQP2 antibody, and intracellular cAMP was measured. [13] IND/MF and IND/GLY/MF combinations synergistically interact in hyperresponsive medium and small airways and modulate the levels of cytokines, neurokinins, ACh, and intracellular cAMP. [14]IM 및 dDAVP 투여 후, 쥐의 신장을 AQP2 항체로 면역염색하고 세포내 cAMP를 측정하였다. [1] 우리의 결과는 OCT에 의한 활성화 SSTR2가 쥐 DRG 뉴런에서 세포내 cAMP 및 PKA 신호 전달 경로를 통해 ASIC의 활성을 억제할 수 있음을 나타냅니다. [2] 더 흥미롭게도, 우리는 TRAF2가 일차 hFLS의 세포질에서 G 단백질 결합 수용체 키나제(GRK2)와 상호작용하고 TNF-α 자극에 반응하여 GRK2를 세포막으로 가져오는 것을 도왔다는 것을 밝혔습니다. 막 및 전위된 GRK2는 EP4의 탈감작 및 내재화를 유도하여 세포내 cAMP의 생산을 감소시켰다. [3] 최근 보고서에 따르면 포스포디에스테라제(PDE) 억제제를 비롯한 세포 내 cAMP 상승 화합물이 유망한 항섬유화제 종류를 나타낼 수 있습니다. [4] forskolin(FSK) 및 3-isobutyl-1-methylxanthine(IBMX)을 사용한 세포 내 cAMP의 자극은 WT 원위 회장 및 맹장에서 순 옥살산 분비를 증가시키고 맹장 및 원위 결장에서 나트륨 흡수를 억제했습니다. [5] PDE4 차단은 세포 내 cAMP 수준을 증가시킬 수 있으며, 이는 종양 괴사 인자(TNF), 인터루킨(IL)-23, IL-17, 인터페론-γ의 발현을 감소시켜 염증 반응의 하향 조절을 초래하는 동시에 조절을 증가시킵니다. IL-10과 같은 사이토카인. [6] PTS 활성은 세포 내 cAMP 수준을 감소시켜 독성 유전자를 상향 조절합니다. [7] 세포 내 cAMP는 HTRF 기반 기술을 사용하여 고립된 섬에서 연구되었습니다. [8] 두 수용체가 모두 존재할 때 LPA2 및/또는 GPR55 활성화는 공동 내재화를 촉진하고 Gαi와 결합되지 않은 GPR55의 활성화는 세포내 cAMP의 감소를 유도했습니다. [9] 실험에서 β1-AR이 갑자기 활성화되면 세포 내 cAMP는 정상 상태 수준으로 수렴하기 전에 일시적으로 고농도로 상승할 수 있습니다. [10] 기능적으로, β3-AR의 감소는 세포내 cAMP, 지방분해 및 지방분해에 의해 활성화된 분리 단백질 1 매개 열발생 능력의 작용제 매개 증가를 낮추었습니다. [11] OT는 세포내 cAMP의 KOR 작용제 유도 Gi/o 단백질 매개 감소를 강화했지만 KOR 작용제 dynorphin A 및 (-)-U-50488 염산염(U50488)에 의한 KOR 내재화의 증가에는 영향을 미치지 않았습니다. [12] IM 및 dDAVP 투여 후, 쥐의 신장을 AQP2 항체로 면역염색하고 세포내 cAMP를 측정하였다. [13] IND/MF 및 IND/GLY/MF 조합은 과민성 중간 및 작은 기도에서 상승적으로 상호작용하고 사이토카인, 뉴로키닌, ACh 및 세포내 cAMP의 수준을 조절합니다. [14]
production dose dependently 생산 용량 의존적으로
Three agonists, [Nle4, D-Phe7]-alpha-melanocyte stimulating hormone (NDP-MSH), alpha-MSH, and adrenocorticotropin (ACTH), could bind to maMC5R and induce intracellular cAMP production dose-dependently. [1] Three agonists, α-melanocyte-stimulating hormone (α-MSH), ACTH (1-24), and [Nle4, D-Phe7]-α-MSH, could bind to maMC5R and induce intracellular cAMP production dose-dependently. [2] The cloned grouper MC4R was functional, exhibiting high constitutive activity in cAMP pathway, capable of binding to three peptide agonists and increasing intracellular cAMP production dose-dependently. [3]세 가지 작용제, [Nle4, D-Phe7]-알파-멜라닌 세포 자극 호르몬(NDP-MSH), 알파-MSH 및 부신피질 자극 호르몬(ACTH)은 maMC5R에 결합하여 용량 의존적으로 세포내 cAMP 생산을 유도할 수 있습니다. [1] 3가지 효능제인 α-멜라닌 세포 자극 호르몬(α-MSH), ACTH(1-24) 및 [Nle4, D-Phe7]-α-MSH는 maMC5R에 결합하여 용량 의존적으로 세포 내 cAMP 생산을 유도할 수 있습니다. [2] nan [3]
dose dependent manner 용량 의존 방식
Conclusions: It was shown that mechanism of K562 cell proliferation inhibition by these compounds is based on CaM and consequent PDE inhibition followed by intracellular cAMP level elevation and increased PKA activity in a dose-dependent manner. [1] Cell-based luciferase reporter assays showed that the three chicken HTRs were functional, capable of binding their natural ligands (5-HT) or selective agonists (CP94253, BRL54443, and LY344864) and inhibiting intracellular cAMP production in a dose-dependent manner. [2] Further pharmacological experiments showed that the cloned snakehead MC4R was functional, capable of binding to peptide agonists and increasing intracellular cAMP production in a dose-dependent manner. [3]결론: 이들 화합물에 의한 K562 세포 증식 억제의 기전은 CaM 및 이에 따른 PDE 억제에 따른 세포내 cAMP 수준 상승 및 용량 의존적 방식으로 증가된 PKA 활성에 기초하는 것으로 나타났다. [1] 세포 기반 루시퍼라제 리포터 분석은 3개의 닭 HTR이 기능적이며 천연 리간드(5-HT) 또는 선택적 작용제(CP94253, BRL54443 및 LY344864)에 결합할 수 있고 용량 의존적 방식으로 세포내 cAMP 생산을 억제할 수 있음을 보여주었습니다. [2] 추가 약리학적 실험은 복제된 뱀머리 MC4R이 기능적이며 펩타이드 작용제에 결합할 수 있고 용량 의존적 방식으로 세포내 cAMP 생산을 증가시킬 수 있음을 보여주었습니다. [3]
Increased Intracellular Camp 증가된 세포내 캠프
Deleting Rgs genes significantly increased intracellular cAMP levels, and caused defects in mycelia growth, stress resistance, conidiation, trap formation, and nematocidal activity. [1] Increased extracellular cAMP levels ([cAMP]e) are long-lived in culture and induced by receptor-dependent and receptor-independent mechanisms in such a way as to define a universal response class of increased intracellular cAMP levels ([cAMP]i). [2] Exposure of these cells to noradrenaline and the β-adrenoceptor agonist isoproterenol increased intracellular cAMP levels and induced the formation of processes. [3] In A498 and 786O cells, treatment with Ang-(1–7) increased intracellular cAMP in a concentrationdependent manner and reduced the number of colonies formed by A498 cells. [4] Here, we found that a dietary saturated fatty acid (FA), palmitate increased intracellular cAMP synthesis through the palmitoylation of soluble adenylyl cyclase in cardiomyocytes. [5] Pre-treatment with PAP increased intracellular cAMP and nicotinamide adenine dinucleotide (NAD+) levels, restored mitochondrial membrane potential (ΔΨm), and decreased ROS and caspase 3/7 content in QUIN exposed neurons. [6] Forskolin increased intracellular cAMP levels and inhibited CTGF expression in MCFs. [7] Using a fusion of the CTF of GPR133 and the N terminus of thrombin-activated human protease-activated receptor 1 as a controllable proxy system to test the effect of intramolecular cleavage and dissociation, we also showed that thrombin-induced cleavage and shedding of the human protease-activated receptor 1 NTF increased intracellular cAMP levels. [8] Our study also found that BCE-BuOH suppressed the expression of phosphodiesterase 4b mRNA, which increased intracellular cAMP levels. [9] Increased intracellular cAMP or inhibition of AMPK prevented both IL-1β-induced NO release and mitochondrial dysfunction. [10] Treating goat LCs with hCG (5 IU/ml) significantly increased intracellular cAMP levels. [11] Furthermore, salidroside increased intracellular cAMP levels, while the PKA-selective inhibitor H-89 attenuated the effects of salidroside on IH-induced RhoA/ROCK suppression, ROS scavenging, and barrier protection. [12] Finally, efficient translocation of SipA-CyaA’ into HeLa cells was evidenced by increased intracellular cAMP levels at different times of infection. [13] Moreover, ROF increased intracellular cAMP level, PKA and HO-1 activities and Nrf2, NQO-1 and HO-1 gene expression, improved testicular oxidative stress parameters (TBARS, NO, GSH levels, and CAT activity) and inflammatory mediators (IL-1β and TNF-α, and NF-κβ p65gene expression) and reduced the proapoptotic proteins, caspase-3, Bax and increased Bcl-2. [14] Moreover, we confirmed that, as in ejaculated crocodile spermatozoa, increased intracellular cAMP levels promoted a significant and sustained enhancement of sperm motility regardless of whether the cells were isolated from the testis or epididymis. [15] Our results further demonstrated that PDE4D deficiency increased intracellular cAMP levels and resulted in downregulation of MAPK but not PI3K/AKT signaling in a CRAF dependent manners. [16] We observed CFE treatment on melanocytes increased intracellular cAMP with inducing pCREB and up-regulating the protein levels of TYR and MITF. [17] DA-1241 increased intracellular cAMP in HIT-T15 insulinoma cells (EC50, 14. [18]Rgs 유전자를 삭제하면 세포 내 cAMP 수준이 크게 증가하고 균사 성장, 스트레스 저항성, 분생자, 트랩 형성 및 선충 활성에 결함이 발생했습니다. [1] 증가된 세포외 cAMP 수준([cAMP]e)은 배양에서 오래 지속되며 증가된 세포내 cAMP 수준([cAMP]i)의 보편적인 반응 클래스를 정의하는 방식으로 수용체 의존적 및 수용체 독립적인 메커니즘에 의해 유도됩니다. [2] nan [3] nan [4] nan [5] nan [6] nan [7] nan [8] nan [9] nan [10] nan [11] nan [12] nan [13] nan [14] nan [15] nan [16] nan [17] nan [18]
Increase Intracellular Camp 세포내 캠프 증가
We further demonstrate that magnesium ion enters osteocytes, increases intracellular cAMP level and activates ATF4, a key transcription factor known to regulate Wnt/β-catenin signaling. [1] We find the E prostanoid receptor 4 expressed in T-ALL samples and demonstrate that prostaglandin E2 (PGE2) increases intracellular cAMP, potentiates GC-induced gene expression, and sensitizes human T-ALL samples to dexamethasone in vitro and in vivo. [2] The vasopressin V2 receptor (V2R), which is a GS protein-coupled receptor that increases intracellular cAMP levels, has a major role in this targeting process. [3] In conclusion, narirutin has vasorelaxing effect and the mechanism involves the inhibition of phosphodiesterase, which increases intracellular cAMP, thereby stimulating the endothelial nitric oxide synthase and activating the voltage-gated potassium channels in vascular smooth muscle cells. [4] Acting via the type 1 PTH receptor, teriparatide and abaloparatide increase intracellular cAMP and induce osteoanabolic effect, and many PDE inhibitors mimic this effect in preclinical studies. [5] All agonists could stimulate ipMC3R and increase intracellular cAMP production with sub-nanomolar potencies. [6] Incubation of blood stream form trypanosomes by 37 increases intracellular cAMP levels and results in the distortion of the cell cycle and cell death, validating phosphodiesterase inhibition as mode of action. [7]우리는 추가로 마그네슘 이온이 골세포에 들어가 세포 내 cAMP 수준을 증가시키며 Wnt/β-카테닌 신호 전달을 조절하는 것으로 알려진 주요 전사 인자인 ATF4를 활성화한다는 것을 보여줍니다. [1] 우리는 T-ALL 샘플에서 발현된 E 프로스타노이드 수용체 4를 발견하고 프로스타글란딘 E2(PGE2)가 세포내 cAMP를 증가시키고 GC-유도 유전자 발현을 강화하며 인간 T-ALL 샘플을 시험관내 및 생체내에서 덱사메타손에 민감하게 한다는 것을 입증합니다. [2] nan [3] nan [4] nan [5] nan [6] nan [7]
Increasing Intracellular Camp 세포내 캠프 증가
Further pharmacological experiments showed that the cloned snakehead MC4R was functional, capable of binding to peptide agonists and increasing intracellular cAMP production in a dose-dependent manner. [1] Hypothesis Increasing intracellular cAMP during LABA/GCS combination therapy via inhibiting phosphodiesterase 4 (PDE4) and/or blocking the export of cAMP by ATP Binding Cassette Transporter C4 (ABCC4), will potentiate anti-inflammatory responses of mainstay LABA/GCS therapy. [2] The cloned grouper MC4R was functional, exhibiting high constitutive activity in cAMP pathway, capable of binding to three peptide agonists and increasing intracellular cAMP production dose-dependently. [3] Increasing intracellular cAMP levels, which preferentially affects HCN4 gating relative to the other isoforms, drove repetitive firing of FCM neurons but not that of control pyramidal neurons. [4]추가 약리학적 실험은 복제된 뱀머리 MC4R이 기능적이며 펩타이드 작용제에 결합할 수 있고 용량 의존적 방식으로 세포내 cAMP 생산을 증가시킬 수 있음을 보여주었습니다. [1] 가설 포스포디에스테라제 4(PDE4) 억제 및/또는 ATP 결합 카세트 트랜스포터 C4(ABCC4)에 의한 cAMP 내보내기 차단을 통해 LABA/GCS 병용 요법 동안 세포내 cAMP를 증가시키면 주요 LABA/GCS 요법의 항염증 반응이 강화될 것입니다. [2] nan [3] nan [4]
Stimulated Intracellular Camp 자극된 세포내 캠프
In contrast, Y-27632 augmented the β-agonist-stimulated intracellular cAMP production. [1] NMU decreased forskolin-stimulated intracellular cAMP in both mouse and human islets. [2] Comparable changes in basal and stimulated intracellular cAMP were also observed. [3]대조적으로, Y-27632는 β-작용제-자극된 세포내 cAMP 생산을 증가시켰다. [1] NMU는 마우스와 인간의 섬 모두에서 포스콜린으로 자극된 세포내 cAMP를 감소시켰습니다. [2] nan [3]
Induce Intracellular Camp 세포내 캠프 유도
Three agonists, [Nle4, D-Phe7]-alpha-melanocyte stimulating hormone (NDP-MSH), alpha-MSH, and adrenocorticotropin (ACTH), could bind to maMC5R and induce intracellular cAMP production dose-dependently. [1] Three agonists, α-melanocyte-stimulating hormone (α-MSH), ACTH (1-24), and [Nle4, D-Phe7]-α-MSH, could bind to maMC5R and induce intracellular cAMP production dose-dependently. [2]세 가지 작용제, [Nle4, D-Phe7]-알파-멜라닌 세포 자극 호르몬(NDP-MSH), 알파-MSH 및 부신피질 자극 호르몬(ACTH)은 maMC5R에 결합하여 용량 의존적으로 세포내 cAMP 생산을 유도할 수 있습니다. [1] 3가지 효능제인 α-멜라닌 세포 자극 호르몬(α-MSH), ACTH(1-24) 및 [Nle4, D-Phe7]-α-MSH는 maMC5R에 결합하여 용량 의존적으로 세포 내 cAMP 생산을 유도할 수 있습니다. [2]
intracellular camp level 세포내 캠프 수준
Deleting Rgs genes significantly increased intracellular cAMP levels, and caused defects in mycelia growth, stress resistance, conidiation, trap formation, and nematocidal activity. [1] Precise manipulation of bacterial intracellular cAMP levels may enable tunable control of twitching motility or virulence, and optogenetic tools are attractive because they afford excellent spatiotemporal resolution and are easy to operate. [2] Intracellular cAMP levels were assessed by ELISA assay. [3] PAC is a flavoprotein that catalyzes the production of cAMP upon illumination with blue light, which enables us to optogenetically manipulate intracellular cAMP levels in various biological systems. [4] We further demonstrate that magnesium ion enters osteocytes, increases intracellular cAMP level and activates ATF4, a key transcription factor known to regulate Wnt/β-catenin signaling. [5] As it would be expected for canonical AVPR2-activation, dDAVP raised intracellular cAMP levels in osteosarcoma cells, and coincubation with phosphodiesterase-inhibitor rolipram indicated synergistic antiproliferative activity. [6] Isorhamnetin did not alter intracellular cAMP levels and the activity of other ion channels, including ANO1, ENaC, and hERG. [7] Increased extracellular cAMP levels ([cAMP]e) are long-lived in culture and induced by receptor-dependent and receptor-independent mechanisms in such a way as to define a universal response class of increased intracellular cAMP levels ([cAMP]i). [8] Moreover, MIA-690 reduced both basal and GHRH-induced secretion of GH and intracellular cAMP levels. [9] This results in an increase in intracellular cAMP levels, playing a role in promoting glycogenolysis and gluconeogenesis, and promoting blood glucose elevation. [10] The vasopressin V2 receptor (V2R), which is a GS protein-coupled receptor that increases intracellular cAMP levels, has a major role in this targeting process. [11] Here, we generated a transgenic mouse line, Mlc1-bPAC, in which astrocytes increase their intracellular cAMP levels upon blue light stimulation. [12] Here we have shown that infection of bone marrow-derived macrophages with H37Rv causes a Cor1 dependent rise of intracellular cAMP levels at the vicinity of the phagosomes. [13] Exposure of these cells to noradrenaline and the β-adrenoceptor agonist isoproterenol increased intracellular cAMP levels and induced the formation of processes. [14] We also show that this phosphorylation is critical for maintaining intracellular cAMP levels in the pulmonary endothelium and endothelial barrier integrity. [15] Although the adenylate cyclase inhibitor 2',5'-dideoxyadenosine suppressed the elevation of intracellular cAMP level induced by PGE2 in the presence of caffeine, it had no effect on the inhibition of HSC activation by PGE2 plus caffeine. [16] cAMP signaling has been studied in ATC for the first time through our study wherein cAMP signaling is downregulated due to decrease in intracellular cAMP level upon metformin treatment. [17] Intracellular cAMP level and the protein expression levels were measured to elucidate the underlying mechanisms. [18] Deletion of Bcgb1 resulted in a significant reduction in the expression of several genes involved in cAMP signaling, and caused a notable increase in intracellular cAMP levels, suggesting that G protein β subunit Bcgb1 plays an important role in cAMP signaling. [19] Interestingly, phosphodiesterase (PDE) 4 inhibitors have been used in human airway diseases characterized by low intracellular cAMP levels and increases in specific cAMP hydrolyzing activity. [20] Forskolin increased intracellular cAMP levels and inhibited CTGF expression in MCFs. [21] Compared with the wild-type strain, Δ Uvcap1 showed decreased tolerance to sorbitol and H 2 O 2 , and increased tolerance to NaCl, CFW and SDS, and the intracellular cAMP level was significantly reduced in Δ Uvcap1. [22] Using a fusion of the CTF of GPR133 and the N terminus of thrombin-activated human protease-activated receptor 1 as a controllable proxy system to test the effect of intramolecular cleavage and dissociation, we also showed that thrombin-induced cleavage and shedding of the human protease-activated receptor 1 NTF increased intracellular cAMP levels. [23] Our study also found that BCE-BuOH suppressed the expression of phosphodiesterase 4b mRNA, which increased intracellular cAMP levels. [24] Conclusions: It was shown that mechanism of K562 cell proliferation inhibition by these compounds is based on CaM and consequent PDE inhibition followed by intracellular cAMP level elevation and increased PKA activity in a dose-dependent manner. [25] In this study, we investigated the specific roles of PDE2A and PDE3B in the regulation of intracellular cAMP levels in different mouse T cell subsets. [26] Treating goat LCs with hCG (5 IU/ml) significantly increased intracellular cAMP levels. [27] Furthermore, salidroside increased intracellular cAMP levels, while the PKA-selective inhibitor H-89 attenuated the effects of salidroside on IH-induced RhoA/ROCK suppression, ROS scavenging, and barrier protection. [28] Mutant Gsα was partially protected from proteolysis after incubation with GTP, indicating diminished GTPase activity and reduced GTP hydrolysis as the mechanism for increased basal intracellular cAMP levels. [29] It is well known that hypoxanthine (HX) inhibits nuclear maturation of oocytes by elevating the intracellular cAMP level, while melatonin (MT) is a molecule that reduces cAMP production, which may physiologically antagonize this inhibition and restore the meiosis process. [30] Finally, efficient translocation of SipA-CyaA’ into HeLa cells was evidenced by increased intracellular cAMP levels at different times of infection. [31] Moreover, ROF increased intracellular cAMP level, PKA and HO-1 activities and Nrf2, NQO-1 and HO-1 gene expression, improved testicular oxidative stress parameters (TBARS, NO, GSH levels, and CAT activity) and inflammatory mediators (IL-1β and TNF-α, and NF-κβ p65gene expression) and reduced the proapoptotic proteins, caspase-3, Bax and increased Bcl-2. [32] Moreover, we confirmed that, as in ejaculated crocodile spermatozoa, increased intracellular cAMP levels promoted a significant and sustained enhancement of sperm motility regardless of whether the cells were isolated from the testis or epididymis. [33] Our results further demonstrated that PDE4D deficiency increased intracellular cAMP levels and resulted in downregulation of MAPK but not PI3K/AKT signaling in a CRAF dependent manners. [34] Intracellular cAMP levels were measured using enzyme immunoassay. [35] Shifting intracellular cAMP levels controls the polarity of microglial responses to changes in brain homeostasis and alters the scale of immunosurveillance. [36] Our data showed that BDE-209 did not change intracellular cAMP level in the presence of human Chorionic Gonadotropin (hCG), cholera toxin (CT), and forskolin, which indicated that reduction of progesterone may not be related to the hCG-cAMP signal pathway in MLTC-1 cells. [37] Next, the effect of 2ccPA on the intracellular cAMP levels was determined to investigate the mechanisms of the antifibrotic activity of 2ccPA. [38] Binding of GLP-1 to its cognate receptor on pancreatic β cells up-regulates intracellular cAMP levels, in turn reducing streptozotocin-induced β-cell death. [39] Our results suggested that although BAI3 played a role in C1QL4‐induced steroidogenesis, there was an unidentified receptor that mediated C1QL4‐activated testosterone secretion in Leydig cells through phosphorylation of ERK1/2 and up‐regulation of intracellular cAMP levels. [40] Incubation of blood stream form trypanosomes by 37 increases intracellular cAMP levels and results in the distortion of the cell cycle and cell death, validating phosphodiesterase inhibition as mode of action. [41] This results in high intracellular cAMP levels, which lead to aberrant renal tubular epithelial cell proliferation and chloride-driven fluid excretion in the kidney, causing cyst formation and growth. [42] Platelet-derived factors did not affect intracellular cAMP levels and phosphorylation of CREB, but activated Smad3 and its downstream-target plasminogen activator inhibitor (PAI)-1 in forskolin-induced BeWo cell differentiation. [43] Increasing intracellular cAMP levels, which preferentially affects HCN4 gating relative to the other isoforms, drove repetitive firing of FCM neurons but not that of control pyramidal neurons. [44] Src inhibition by Das did not change the intracellular cAMP levels. [45]Rgs 유전자를 삭제하면 세포 내 cAMP 수준이 크게 증가하고 균사 성장, 스트레스 저항성, 분생자, 트랩 형성 및 선충 활성에 결함이 발생했습니다. [1] 박테리아 세포 내 cAMP 수준의 정확한 조작은 경련 운동성 또는 독성의 조정 가능한 제어를 가능하게 할 수 있으며 광유전학 도구는 우수한 시공간 해상도를 제공하고 작동하기 쉽기 때문에 매력적입니다. [2] 세포내 cAMP 수준을 ELISA 분석에 의해 평가하였다. [3] nan [4] 우리는 추가로 마그네슘 이온이 골세포에 들어가 세포 내 cAMP 수준을 증가시키며 Wnt/β-카테닌 신호 전달을 조절하는 것으로 알려진 주요 전사 인자인 ATF4를 활성화한다는 것을 보여줍니다. [5] nan [6] nan [7] 증가된 세포외 cAMP 수준([cAMP]e)은 배양에서 오래 지속되며 증가된 세포내 cAMP 수준([cAMP]i)의 보편적인 반응 클래스를 정의하는 방식으로 수용체 의존적 및 수용체 독립적인 메커니즘에 의해 유도됩니다. [8] 더욱이, MIA-690은 GH 및 세포내 cAMP 수준의 기저 및 GHRH 유도 분비를 모두 감소시켰다. [9] 이는 세포내 cAMP 수준의 증가를 초래하여 글리코겐분해 및 포도당신생합성을 촉진하고 혈당 상승을 촉진하는 역할을 합니다. [10] nan [11] 여기에서 우리는 성상세포가 청색광 자극 시 세포내 cAMP 수준을 증가시키는 형질전환 마우스 라인인 Mlc1-bPAC를 생성했습니다. [12] 여기에서 우리는 H37Rv에 의한 골수 유래 대식세포의 감염이 포식소체 부근에서 세포내 cAMP 수준의 Cor1 의존적 상승을 유발한다는 것을 보여주었다. [13] nan [14] nan [15] adenylate cyclase inhibitor 2',5'-dideoxyadenosine은 카페인 존재하에서 PGE2에 의해 유도된 세포내 cAMP 수치의 상승을 억제했지만, PGE2와 카페인에 의한 HSC 활성화 억제에는 효과가 없었다. [16] cAMP 신호는 메트포르민 치료 시 세포 내 cAMP 수준의 감소로 인해 cAMP 신호가 하향 조절된다는 우리 연구를 통해 ATC에서 처음으로 연구되었습니다. [17] 세포 내 cAMP 수준과 단백질 발현 수준을 측정하여 기본 메커니즘을 설명했습니다. [18] Bcgb1의 삭제는 cAMP 신호 전달에 관여하는 여러 유전자의 발현을 현저하게 감소시켰고 세포 내 cAMP 수준의 현저한 증가를 초래하여 G 단백질 β 소단위 Bcgb1이 cAMP 신호 전달에서 중요한 역할을 함을 시사합니다. [19] nan [20] nan [21] Δ Uvcap1은 야생형 균주와 비교하여 소르비톨 및 H 2 O 2 에 대한 내성이 감소하고 NaCl, CFW 및 SDS에 대한 내성이 증가하였으며, Δ Uvcap1에서는 세포내 cAMP 수준이 유의하게 감소하였다. [22] nan [23] nan [24] 결론: 이들 화합물에 의한 K562 세포 증식 억제의 기전은 CaM 및 이에 따른 PDE 억제에 따른 세포내 cAMP 수준 상승 및 용량 의존적 방식으로 증가된 PKA 활성에 기초하는 것으로 나타났다. [25] 이 연구에서 우리는 다른 마우스 T 세포 하위 집합에서 세포 내 cAMP 수준의 조절에서 PDE2A와 PDE3B의 특정 역할을 조사했습니다. [26] nan [27] nan [28] nan [29] 하이포크산틴(HX)은 세포 내 cAMP 수준을 높여 난모세포의 핵 성숙을 억제하는 반면 멜라토닌(MT)은 cAMP 생산을 감소시키는 분자로 생리학적으로 이러한 억제를 길항하고 감수 분열 과정을 회복시킬 수 있습니다. [30] nan [31] nan [32] nan [33] nan [34] nan [35] nan [36] nan [37] nan [38] nan [39] nan [40] nan [41] nan [42] nan [43] nan [44] nan [45]
intracellular camp production 세포내 캠프 생산
In contrast, Y-27632 augmented the β-agonist-stimulated intracellular cAMP production. [1] The responses of intracellular cAMP production, aquaporin-2 (AQP2) protein expression and localization, vasopressin-2 receptor (V2R) and AQP2 mRNA, and cAMP-responsive element binding protein (CREB) were tested with and without tolvaptan, and the protein kinase A (PKA) inhibitors H89 and Rp-cAMPS. [2] Adenosine A2A receptor activation in the donor cells using a selective agonist results in intracellular cAMP production. [3] Three agonists, [Nle4, D-Phe7]-alpha-melanocyte stimulating hormone (NDP-MSH), alpha-MSH, and adrenocorticotropin (ACTH), could bind to maMC5R and induce intracellular cAMP production dose-dependently. [4] Cell-based luciferase reporter assays showed that the three chicken HTRs were functional, capable of binding their natural ligands (5-HT) or selective agonists (CP94253, BRL54443, and LY344864) and inhibiting intracellular cAMP production in a dose-dependent manner. [5] Three agonists, α-melanocyte-stimulating hormone (α-MSH), ACTH (1-24), and [Nle4, D-Phe7]-α-MSH, could bind to maMC5R and induce intracellular cAMP production dose-dependently. [6] Further pharmacological experiments showed that the cloned snakehead MC4R was functional, capable of binding to peptide agonists and increasing intracellular cAMP production in a dose-dependent manner. [7] The cloned grouper MC4R was functional, exhibiting high constitutive activity in cAMP pathway, capable of binding to three peptide agonists and increasing intracellular cAMP production dose-dependently. [8] All agonists could stimulate ipMC3R and increase intracellular cAMP production with sub-nanomolar potencies. [9]대조적으로, Y-27632는 β-작용제-자극된 세포내 cAMP 생산을 증가시켰다. [1] 세포 내 cAMP 생산, aquaporin-2(AQP2) 단백질 발현 및 국소화, 바소프레신-2 수용체(V2R) 및 AQP2 mRNA, cAMP-반응성 요소 결합 단백질(CREB)의 반응을 톨밥탄의 유무에 관계없이 시험하였다. A(PKA) 억제제 H89 및 Rp-cAMPS. [2] 선택적 작용제를 사용하는 공여자 세포에서 아데노신 A2A 수용체 활성화는 세포내 cAMP 생산을 초래합니다. [3] 세 가지 작용제, [Nle4, D-Phe7]-알파-멜라닌 세포 자극 호르몬(NDP-MSH), 알파-MSH 및 부신피질 자극 호르몬(ACTH)은 maMC5R에 결합하여 용량 의존적으로 세포내 cAMP 생산을 유도할 수 있습니다. [4] 세포 기반 루시퍼라제 리포터 분석은 3개의 닭 HTR이 기능적이며 천연 리간드(5-HT) 또는 선택적 작용제(CP94253, BRL54443 및 LY344864)에 결합할 수 있고 용량 의존적 방식으로 세포내 cAMP 생산을 억제할 수 있음을 보여주었습니다. [5] 3가지 효능제인 α-멜라닌 세포 자극 호르몬(α-MSH), ACTH(1-24) 및 [Nle4, D-Phe7]-α-MSH는 maMC5R에 결합하여 용량 의존적으로 세포 내 cAMP 생산을 유도할 수 있습니다. [6] 추가 약리학적 실험은 복제된 뱀머리 MC4R이 기능적이며 펩타이드 작용제에 결합할 수 있고 용량 의존적 방식으로 세포내 cAMP 생산을 증가시킬 수 있음을 보여주었습니다. [7] nan [8] nan [9]
intracellular camp signaling 세포내 캠프 신호
PDE7 is involved in many important functional processes in physiology and pathology by regulating intracellular cAMP signaling. [1] It is also known that intracellular cAMP signaling is highly compartmentalized into small nanodomains and localized cAMP changes are sufficient at modifying the permeability of the endothelial barrier. [2] Our results demonstrate class‐specific and individual C‐terminal motif equipment of odorant receptors, which instruct their functional expression in a test cell system, and in situ may regulate their individual cell surface expression and intracellular cAMP signaling. [3] Extracellular and intracellular cAMP signaling are essential to many developmental processes. [4]PDE7은 세포내 cAMP 신호전달을 조절함으로써 생리학 및 병리학에서 많은 중요한 기능적 과정에 관여합니다. [1] 또한 세포내 cAMP 신호전달이 작은 나노도메인으로 고도로 구획화되어 있고 국소화된 cAMP 변화가 내피 장벽의 투과성을 수정하는 데 충분하다는 것도 알려져 있습니다. [2] 우리의 결과는 시험 세포 시스템에서 기능적 발현을 지시하고 제자리에서 개별 세포 표면 발현과 세포 내 cAMP 신호를 조절할 수 있는 냄새 수용체의 클래스 특이적 및 개별 C-말단 모티프 장비를 보여줍니다. [3] 세포외 및 세포내 cAMP 신호전달은 많은 발달 과정에 필수적입니다. [4]
intracellular camp receptor 세포내 캠프 수용체
Introduction: Intracellular cAMP receptor exchange proteins directly activated by cAMP 1 (EPAC1) regulate obligate intracellular parasitic bacterium rickettsial adherence to and invasion into vascular endothelial cells (ECs). [1] Another intracellular cAMP receptor, EPAC, was not involved in IL-6 release. [2] Moreover, we reported that intracellular cAMP receptor EPAC1 modulates ANXA2 tyrosine (Y) 23 phosphorylation, and inactivation of EPAC1 suppresses ANXA2 expression on the EC luminal surface by downregulating Y23 phosphorylation. [3] The exchange protein directly activated by cAMP (EPAC) is a ubiquitously expressed intracellular cAMP receptor that plays a regulatory role in suppressing inflammation. [4]소개: cAMP 1(EPAC1)에 의해 직접 활성화된 세포 내 cAMP 수용체 교환 단백질은 혈관 내피 세포(EC)에 대한 절대 세포 내 기생 박테리아 리케차 부착 및 침입을 조절합니다. [1] 또 다른 세포내 cAMP 수용체인 EPAC는 IL-6 방출에 관여하지 않았다. [2] 또한, 우리는 세포 내 cAMP 수용체 EPAC1이 ANXA2 티로신(Y) 23 인산화를 조절하고 EPAC1의 비활성화가 Y23 인산화를 하향 조절함으로써 EC 내강 표면에서 ANXA2 발현을 억제한다고 보고했습니다. [3] nan [4]
intracellular camp generation 세포내 캠프 생성
Intracellular cAMP generation was determined by radioimmunoassay and caMC3R expression was quantified with flow cytometry. [1] Liver-specific Expression of Constitutively Active Gsα Leads to Hyperglycemia With Impaired Insulin Secretion The ubiquitously-expressed G protein Gsα couples hormone receptors to the stimulation of intracellular cAMP generation. [2] Objective Gsα couples multiple receptors, including the melanocortin 4 receptor (MC4R), to intracellular cAMP generation. [3]세포내 cAMP 생성은 방사성면역분석에 의해 결정되었고 caMC3R 발현은 유세포분석으로 정량화되었다. [1] 구성적으로 활성인 Gsα의 간 특이적 발현은 인슐린 분비 장애를 동반한 고혈당증을 유발합니다. 편재적으로 발현되는 G 단백질 Gsα는 호르몬 수용체를 세포내 cAMP 생성의 자극에 연결합니다. [2] nan [3]
intracellular camp content 세포내 캠프 콘텐츠
We found that intracellular cAMP content increased but PKA content decreased in ΔAaPKAc mutant strain. [1] GLA, DGLA, AA, EPA and DHA and prostaglandin E2 (PGE2), lipoxin A4 (LXA4) (pro- and anti-inflammatory metabolites of AA respectively) activate/suppress various SIRTs (SIRt1 SIRT2, SIRT3, SIRT4, SIRT5, SIRT6), PPAR-γ, PARP, p53, SREBP1, intracellular cAMP content, PKA activity and peroxisome proliferator-activated receptor γ coactivator 1-α (PGC1-α). [2] Extracellular ligand binding to seven-transmembrane receptors (also known as GPCRs) with G proteins and adenylyl cyclases (ACs) modulate the intracellular cAMP content. [3]우리는 ΔAaPKAc 돌연변이 균주에서 세포 내 cAMP 함량이 증가하지만 PKA 함량이 감소한다는 것을 발견했습니다. [1] GLA, DGLA, AA, EPA 및 DHA 및 프로스타글란딘 E2(PGE2), 리폭신 A4(LXA4)(각각 AA의 염증 촉진 및 항염 대사 산물)는 다양한 SIRT(SIRt1 SIRT2, SIRT3, SIRT4, SIRT5, SIRT6)를 활성화/억제합니다. , PPAR-γ, PARP, p53, SREBP1, 세포내 cAMP 함량, PKA 활성 및 과산화소체 증식제 활성화 수용체 γ 보조 활성화제 1-α(PGC1-α). [2] G 단백질 및 아데닐릴 사이클라제(AC)를 사용하여 7개 막횡단 수용체(GPCR이라고도 함)에 결합하는 세포외 리간드는 세포내 cAMP 함량을 조절합니다. [3]
intracellular camp concentration 세포내 캠프 농도
While intracellular cAMP concentration did not increase during capacitation in Slc22a14 KO spermatozoa, HCO3--dependent soluble adenylate cyclase activity was normal, and the addition of 8-bromo cAMP rescued the decreased protein tyrosine phosphorylation. [1] Here, I review studies revealing that (sub)anesthetic doses of ketamine elevate intracellular cAMP concentration ([cAMP]i) in astrocytes, attenuate stimulus-evoked astrocyte calcium signaling, which regulates exocytotic secretion of gliosignaling molecules, and stabilize the vesicle fusion pore in a narrow configuration, possibly hindering cargo discharge or vesicle recycling. [2] Background Dysfunction of cyclic nucleotide phosphodiesterase 7 (PDE7) has been associated with excess intracellular cAMP concentrations, fueling pathogenic processes that are implicated in neurodegenerative disorders. [3]세포내 cAMP 농도는 Slc22a14 KO 정자에서 capacitation 동안 증가하지 않았지만 HCO3 의존성 가용성 아데닐산 사이클라제 활성은 정상이었고 8-bromo cAMP의 첨가는 감소된 단백질 티로신 인산화를 구제하였다. [1] 여기에서 나는 케타민의 (미)마취 용량이 성상교세포의 세포내 cAMP 농도([cAMP]i)를 높이고, 교시 신호 분자의 세포외 분비를 조절하는 자극 유발 성상세포 칼슘 신호를 약화시키며, 좁은 구성으로 화물 배출 또는 소포 재활용을 방해할 수 있습니다. [2] nan [3]
intracellular camp accumulation 세포내 캠프 축적
In the present paper, we focus on ADCY10 localization and a kinetic analysis of intracellular cAMP accumulation in response to human LH in the absence or presence of four different ADCY10 inhibitors (KH7, LRE1, 2-CE and 4-CE) in MTLC-1 cells. [1] Cellular signalling studies show that the activated receptors can evoke Ca2+-mobilization, pertussis toxin-sensitive ERK phosphorylation, and intracellular cAMP accumulation, which suggests the partecipation of several G protein subtypes, such as Gq/11, Gi/o and Gs. [2]본 논문에서 우리는 MTLC-1에서 4가지 다른 ADCY10 억제제(KH7, LRE1, 2-CE 및 4-CE)의 부재 또는 존재하에 인간 LH에 대한 반응으로 ADCY10 국소화 및 세포내 cAMP 축적의 동역학 분석에 초점을 맞춥니다. 세포. [1] 세포 신호 연구에 따르면 활성화된 수용체는 Ca2+ 동원, 백일해 독소에 민감한 ERK 인산화 및 세포 내 cAMP 축적을 유발할 수 있으며, 이는 Gq/11, Gi/o 및 G와 같은 여러 G 단백질 하위 유형의 참여를 시사합니다. [2]